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- PDB-7bzw: Structure of Hsp21 -

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Basic information

Entry
Database: PDB / ID: 7bzw
TitleStructure of Hsp21
ComponentsHeat shock protein 21, chloroplasticHeat shock response
KeywordsCHAPERONE / small heat shock protein
Function / homology
Function and homology information


chloroplast nucleoid / chloroplast organization / protein folding chaperone complex / response to light stimulus / : / response to heat / regulation of DNA-templated transcription
Similarity search - Function
Heat shock protein 21-like / Hsp20/alpha crystallin family / Small heat shock protein (sHSP) domain profile. / Alpha crystallin/Hsp20 domain / HSP20-like chaperone
Similarity search - Domain/homology
Heat shock protein 21, chloroplastic
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.6 Å
AuthorsLau, W.C.Y.
Funding support Hong Kong, 1items
OrganizationGrant numberCountry
The University Grants Committee, Research Grants Council (RGC)14105517 Hong Kong
CitationJournal: Nat Commun / Year: 2021
Title: Structural basis of substrate recognition and thermal protection by a small heat shock protein.
Authors: Chuanyang Yu / Stephen King Pong Leung / Wenxin Zhang / Louis Tung Faat Lai / Ying Ki Chan / Man Chit Wong / Samir Benlekbir / Yong Cui / Liwen Jiang / Wilson Chun Yu Lau /
Abstract: Small heat shock proteins (sHsps) bind unfolding proteins, thereby playing a pivotal role in the maintenance of proteostasis in virtually all living organisms. Structural elucidation of sHsp- ...Small heat shock proteins (sHsps) bind unfolding proteins, thereby playing a pivotal role in the maintenance of proteostasis in virtually all living organisms. Structural elucidation of sHsp-substrate complexes has been hampered by the transient and heterogeneous nature of their interactions, and the precise mechanisms underlying substrate recognition, promiscuity, and chaperone activity of sHsps remain unclear. Here we show the formation of a stable complex between Arabidopsis thaliana plastid sHsp, Hsp21, and its natural substrate 1-deoxy-D-xylulose 5-phosphate synthase (DXPS) under heat stress, and report cryo-electron microscopy structures of Hsp21, DXPS and Hsp21-DXPS complex at near-atomic resolution. Monomeric Hsp21 binds across the dimer interface of DXPS and engages in multivalent interactions by recognizing highly dynamic structural elements in DXPS. Hsp21 partly unfolds its central α-crystallin domain to facilitate binding of DXPS, which preserves a native-like structure. This mode of interaction suggests a mechanism of sHsps anti-aggregation activity towards a broad range of substrates.
History
DepositionApr 28, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 28, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 13, 2021Group: Database references / Category: citation / citation_author / database_2
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

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Assembly

Deposited unit
1: Heat shock protein 21, chloroplastic
2: Heat shock protein 21, chloroplastic
3: Heat shock protein 21, chloroplastic
4: Heat shock protein 21, chloroplastic
5: Heat shock protein 21, chloroplastic
6: Heat shock protein 21, chloroplastic
7: Heat shock protein 21, chloroplastic
8: Heat shock protein 21, chloroplastic
9: Heat shock protein 21, chloroplastic
10: Heat shock protein 21, chloroplastic
11: Heat shock protein 21, chloroplastic
12: Heat shock protein 21, chloroplastic


Theoretical massNumber of molelcules
Total (without water)283,85512
Polymers283,85512
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein
Heat shock protein 21, chloroplastic / Heat shock response / 25.3 kDa heat shock protein / chloroplastic / AtHsp25.3


Mass: 23654.545 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: HSP21, HSP25.3, At4g27670, T29A15.160 / Production host: Escherichia coli (E. coli) / References: UniProt: P31170

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Hsp21 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 0.25 MDa / Experimental value: NO
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 45 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: T (tetrahedral)
3D reconstructionResolution: 4.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 104126 / Symmetry type: POINT

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